Information on EC 5.3.1.8 - Mannose-6-phosphate isomerase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.3.1.8
-
RECOMMENDED NAME
GeneOntology No.
Mannose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldose-ketose-isomerization
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,5-anhydrofructose degradation
-
-
Amino sugar and nucleotide sugar metabolism
-
-
beta-1,4-D-mannosyl-N-acetyl-D-glucosamine degradation
-
-
Biosynthesis of secondary metabolites
-
-
D-mannose degradation
-
-
d-mannose degradation
-
-
Fructose and mannose metabolism
-
-
GDP-mannose biosynthesis
-
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
-
mannan degradation
-
-
mannitol biosynthesis
-
-
mannitol degradation II
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
D-mannose-6-phosphate aldose-ketose-isomerase
A zinc protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-88-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
strain CGMCC2428
-
-
Manually annotated by BRENDA team
Alcaligenes sp. CGMCC2428
strain CGMCC2428
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain YJ-407, gene pmi1
UniProt
Manually annotated by BRENDA team
strain YJ-407, gene pmi1
UniProt
Manually annotated by BRENDA team
enzyme from Bacillus subtilis strain HB002; ATCC 23857
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
different cultivars, gene pmi
-
-
Manually annotated by BRENDA team
cultivar Suzhouqing
UniProt
Manually annotated by BRENDA team
strain J2315, bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
Manually annotated by BRENDA team
type II enzyme, bifunctional protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
SwissProt
Manually annotated by BRENDA team
Cassia coluteoides
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Microorganisms
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PAO1. Bifunctional enzyme with phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
-
-
Manually annotated by BRENDA team
DSM 3638
-
-
Manually annotated by BRENDA team
bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
Manually annotated by BRENDA team
bifunctional enzyme with mannose-6-phosphate isomerase and sugar-1-phosphate nucleotidylyltransferase activities, EC 5.3.1.8 and EC 2.7.7.13, respectively
GenBank
Manually annotated by BRENDA team
strain DJ77, gene pmi
-
-
Manually annotated by BRENDA team
strain DJ77, gene pmi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-fructose 6-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
show the reaction diagram
D-Allose
D-Psicose
show the reaction diagram
D-Fructose 6-phosphate
?
show the reaction diagram
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
D-Lyxose
D-Xylulose
show the reaction diagram
D-Mannose
D-Fructose
show the reaction diagram
D-Mannose 6-phosphate
?
show the reaction diagram
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
D-Ribose
D-Ribulose
show the reaction diagram
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D-talose
D-tagatose
show the reaction diagram
L-allose
L-psicose
show the reaction diagram
L-Lyxose
L-Xylulose
show the reaction diagram
L-Mannose
L-Fructose
show the reaction diagram
L-ribose
L-ribulose
show the reaction diagram
L-ribulose
L-ribose
show the reaction diagram
L-talose
L-tagatose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Fructose 6-phosphate
?
show the reaction diagram
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9GRS9
first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates
-
r
D-Mannose 6-phosphate
?
show the reaction diagram
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-dipyridyl
2,3-Butanedione
-
inactivation
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
5-deoxy-5-malonyl-D-arabinonohydroxamic acid
-
-
-
5-deoxy-5-phosphonomethyl-D-arabinonate
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
5-phospho-D-arabinonhydrazide
5-phospho-D-arabinonohydroxamic acid
5-phosphoarabinonate
-
6-deoxy-6-carboxymethyl-D-mannose
6-deoxy-6-dicarboxymethyl-D-mannose
6-deoxy-6-dimethylmalonate-D-mannopyranose
6-deoxy-6-phosphonomethyl-D-mannose
6-phospho-2-deoxygluconate
Cassia coluteoides
-
competitive
6-phosphogluconate
6-Phosphomannonate
Cassia coluteoides
-
competitive
8-hydroxyquinoline
-
-
ADP-glucose
-
0.5 mM, 77.8% of initial activity
Ag+
-
irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
alpha-D-mannose 6-phosphate
-
poor
arabinose 5-phosphate
Ba2+
about 30% inhibition at 0.5 mM
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
D-mannose 1-phosphate
-
0.5 mM, 81.9% of initial activity
diethyldicarbonate
-
-
dithiothreitol
erythrose 4-phosphate
Fe2+
-
12% residual activity at 0.5 mM
fructose 1-phosphate
-
competitive
Galactose 6-hosphate
-
competitive
-
GDP-D-mannose
-
inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway
GDP-mannose
-
0.5 mM, 46.7% of initial activity
glucosamine 6-phosphate
-
competitive
glucose 1-phosphate
-
competitive
glucose 6-phosphate
-
competitive
L-ascorbic acid
-
1 mM, 77% residual activity
mannitol 1-phosphate
N,2,3,4,5-pentahydroxypentanamide
-
-
p-chloromercuribenzoate
-
0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity
phosphate
-
competitive
ribose 5-phosphate
-
competitive
S-nitroso-acetyl-penicillamine
-
dose- and time-dependent inactivation
Silver sulfadiazine
sorbitol 6-phosphate
-
competitive
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Co2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
diphosphate
-
0.5 mM, 120% of initial activity
Mg2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Mn2+
-
Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
Ni2+
-
order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043 - 0.33
beta-D-mannose 6-phosphate
0.06 - 0.44
D-fructose 6-phosphate
0.72 - 3.5
D-glucose 6-phosphate
433
D-Lyxose
pH 7.5, 40C, recombinant enzyme
946
D-mannose
pH 7.5, 40C, recombinant enzyme
0.0413 - 243
D-mannose 6-phosphate
110
D-ribose
pH 7.5, 40C, recombinant enzyme
469
D-talose
pH 7.5, 40C, recombinant enzyme
312
L-allose
pH 7.5, 40C, recombinant enzyme
998
L-ribose
pH 7.5, 40C, recombinant enzyme
136 - 308
L-ribulose
0.17 - 4
mannose 6-phosphate
additional information
additional information
-
enzyme kinetics with D-lyxose and L-ribose, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 23
beta-D-mannose 6-phosphate
141
D-fructose 6-phosphate
Thermus thermophilus
Q5SIM4
wild type enzyme, pH 7.0, 80C
7089
D-Lyxose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
3748
D-mannose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
0.076 - 112100
D-mannose 6-phosphate
72
D-ribose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
63970
D-talose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
920
L-allose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
17600
L-ribose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
32670 - 81060
L-ribulose
121 - 162
mannose 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70 - 840
beta-D-mannose 6-phosphate
641
D-fructose 6-phosphate
Thermus thermophilus
Q5SIM4
wild type enzyme, pH 7.0, 80C
87
16.4
D-Lyxose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
1589
3.5
D-mannose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
216
13 - 6685
D-mannose 6-phosphate
0.6
D-ribose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
292
6.8
D-talose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
2017
2.9
L-allose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
10165
17.6
L-ribose
Bacillus subtilis
Q9AGZ4
pH 7.5, 40C, recombinant enzyme
3127
182 - 579
L-ribulose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.162
5-deoxy-5-malonyl-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25C
-
0.0006 - 0.002
5-phospho-D-arabinonhydrazide
0.000041 - 0.0008
5-phospho-D-arabinonohydroxamic acid
0.0105 - 0.115
6-deoxy-6-dicarboxymethyl-D-mannose
0.11 - 58
6-phosphogluconate
0.035 - 0.164
erythrose 4-phosphate
0.0014
erythrose-4-phosphate
-
pH 7.4, 50C
10
N,2,3,4,5-pentahydroxypentanamide
-
in 50 mM HEPES buffer, pH 7.1, at 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
5-deoxy-5-phosphonomethyl-D-arabinonate
0.37 - 2.2
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
0.9 - 4.6
6-deoxy-6-carboxymethyl-D-mannose
0.0181 - 0.199
6-deoxy-6-dicarboxymethyl-D-mannose
1.61 - 4.7
6-deoxy-6-phosphonomethyl-D-mannose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80C
0.0101
recombinant enzyme
0.0165
recombinant enzyme
0.0225
recombinant enzyme
0.0659
recombinant enzyme
0.0918
recombinant enzyme
0.269
-
enzyme activity in cells after 54 h growth on maltose
0.3
mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
0.306
-
enzyme activity in cells after 54 h growth on sucrose
0.313
-
enzyme activity in cells after 54 h growth on glucose
0.6
mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
0.74
wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80C
1.4
mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.5
mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.7
mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
1.9
mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
2.1
mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
2.8
mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
3 - 8
mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
3
-
wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75C
4.5
wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80C
11
mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
19
-
wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75C
22
-
wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75C
23
-
wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75C
31
mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
39
mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
40
mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
42
-
wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75C
44
mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
51
mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
57
-
wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75C
63
-
wild type enzyme, using L-talose as substrate, at pH 7.0 and 75C
80
-
-
85
-
wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75C
126
-
wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75C
128
-
wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75C
165
-
wild type enzyme, using D-allose as substrate, at pH 7.0 and 75C
167
-
wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75C
194
mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80C
333
-
wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75C
425
-
wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75C
474
-
mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75C
742
-
wild type enzyme, using L-allose as substrate, at pH 7.0 and 75C
838
-
mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75C
842
-
wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75C
890
-
purified recombinant enzyme
972
-
mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75C
1011
-
mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75C
1016
-
mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75C
1045
-
mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75C
1046
-
mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75C
1065
-
mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75C
1076
-
mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75C
1092
-
mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75C
1194
-
mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75C
1214
-
mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75C
1270
-
mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75C
1482
-
mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75C
1493
-
wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75C
1619
-
wild type enzyme, using D-talose as substrate, at pH 7.0 and 75C
1791
-
mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75C
2152
-
mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75C
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
about 50% of maximal activity at pH 5.5 and pH 9.0
6 - 11
Cassia coluteoides
-
pH 6.0: 50% of maximal activity, relative high activity up to pH 11
6.3 - 8.8
-
more than 50% of maximum activity in this range
6.5 - 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
recombinant enzyme
75
-
maximal activity of the recombinant enzyme for L-ribulose isomerization
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
growth on liquid and solid media, but no in presence of 90 mM mannose. After transfer of sucrose-grown cell onto medium containing mannose, cells grew little initially, but after a month lag period, they start to form callus colonies. Mannose-accomodated cells are capable of converting mannose to sucrose, with enhanced phosphomannose isomerase activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
Cassia coluteoides
-
developing and germinating
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
gel filtration
29100
gel filtration
36000
-
gel filtration, recombinant enzyme
36600
gel filtration, recombinant enzyme
46520
-
calculation from nucleotide sequence encoded by cDNA
46530
-
recombinant enzyme, electrospray mass spectroscopy
48000
gel filtration
48740
-
wild-type recombinant enzyme, electrospray mass spectroscopy
49060
-
selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy
53000
-
SDS-PAGE
58000
-
gel filtration
59000
-
gel filtration
63000
-
gel filtration
65000
-
sedimentation equilibrium, analytical ultracentrifugation
68000
Cassia coluteoides
-
enzyme from pods, gel filtration
74500
Cassia coluteoides
-
enzyme from pods and seeds, density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and refinement by energy minimization and molecular dynamics
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
both native form and in complex with 5-phosphoarabinonate
enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement
to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomerase
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
40C, 1 h, about 35% loss of activity
2810
6 - 9.5
-
40C, 1 h, no loss of activity
2810
6.5 - 8
-
4C, stable
2827
10
-
40C, 1 h, about 25% loss of activity
2810
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
purified recombinant enzyme, half-life is 461 h
28
-
half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min
30
purified recombinant enzyme, half-life is 325 h
35
purified recombinant enzyme, half-life is 236 h
37
-
6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity
50
purified recombinant enzyme, half-life is 10 h
55
-
pH 6.5, 10 min, about 75% loss of native enzyme
60
-
enzyme half-life is 388 h
64 - 85
the half-lives of the enzyme at 65, 70, 75, 80, and 85C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively
65
-
enzyme half-life is 73 h
65 - 85
-
the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85C, respectively
70
-
enzyme half-life is 27 h
100
-
melting temperature for thermal unfolding, 60 min, 50% residual activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap HP column chromatography
HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatography
-
Ni-affinity column
-
normal and selenomethionine-labelled enzyme expressed in Escherichia coli
-
recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatography
recombinant enzyme 8.7fold from Escherichia coli strain ER2566
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Agrobacterium-based expression in Linum usitatissimum
-
cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli
-
expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain
-
expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli GI724 cells
-
expressed in Nicotiana tabacum transformed with Agrobacterium tumefaciens
expressed in Oryza sativa ssp. japonica varieties Wanjing97 and Nipponbare
-
expression in Agrobacterium tumefaciens
expression in Brassica rapa
-
expression in Escherichia coli
expression in Escherichia coli strain ER2566
expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomerase
-
expression in Pseudomonas aeruginosa
-
gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
high level expression in Escherichia coli M15 as inclusion bodies
overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coli
-
overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosa
-
overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
use of enzyme as selectable marker
-
wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C150A
-
mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition
L129F
the activity of the mutant is 204% of the activity of the wild type enzyme
L129W
the activity of the mutant is 10% of the activity of the wild type enzyme
L129Y
the activity of the mutant is 94% of the activity of the wild type enzyme
N90A/L129F
the activity of the mutant is about 6fold higher than the activity of the wild type enzyme
W17Q/N90A/L129F
the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70C in the presence of 1mM Co2+
E410A
-
about 25% of wild-type catalytic efficiency
E458A
-
about 25% of wild-type catalytic efficiency
H411A
-
about 25% of wild-type catalytic efficiency
N433A
-
about 25% of wild-type catalytic efficiency
R373A
-
about 4% of wild-type catalytic efficiency
R408A
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R408K
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R472A
-
about 1% of wild-type catalytic efficiency
R479A
-
about 3% of wild-type catalytic efficiency
E410A
-
about 25% of wild-type catalytic efficiency
-
H411A
-
about 25% of wild-type catalytic efficiency
-
R408A
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
R408K
-
complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
-
R479A
-
about 3% of wild-type catalytic efficiency
-
E132D
the mutant shows 0.4% activity compared to the wild type enzyme
E67D
the mutant shows 3.7% activity compared to the wild type enzyme
E67Q
the mutant shows 0.8% activity compared to the wild type enzyme
H122Q
the mutant shows 2.0% activity compared to the wild type enzyme
H50Q
the mutant shows 2.0% activity compared to the wild type enzyme
L124A
-
the enzyme shows decreased specific activity for L-ribulose
R142E
-
the enzyme shows decreased specific activity for L-ribulose
R142Q
-
the enzyme shows decreased specific activity for L-ribulose
R142Y
-
the enzyme shows decreased specific activity for L-ribulose
W13F
the mutant shows 41% activity compared to the wild type enzyme
W13H
the mutant shows 52% activity compared to the wild type enzyme
W13Y
the mutant shows 68% activity compared to the wild type enzyme
Y124A
the mutant shows 52% activity compared to the wild type enzyme
E132A
-
the mutants has no activity for L-ribulose; the mutant shows 1.9% activity compared to the wild type enzyme
-
E132D
-
the mutant shows 0.4% activity compared to the wild type enzyme
-
E132Q
-
inactive
-
H122A
-
the mutants has no activity for L-ribulose; the mutant shows 2.8% activity compared to the wild type enzyme
-
K37A
-
the enzyme shows decreased specific activity for L-ribulose; the mutant shows 21% activity compared to the wild type enzyme
-
R11A
-
the enzyme shows about wild type specific activity for L-ribulose
-
R142K
-
the enzyme shows decreased specific activity for L-ribulose
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
development and optimization of a transformation method using the phosphomannose-isomerase gene pmi as a selectable marker for Brassica napus transformation via Agrobacterium tumefaciens, overview
biotechnology
pharmacology
synthesis